• 한국자원식물학회:학술대회논문집
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• 한국자원식물학회 2001년도 The 8th International Symposium
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• pp.63-67
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• 2001

• 한국자원식물학회:학술대회논문집
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• 한국자원식물학회 2001년도 추계정기 학술발표회 초록집
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• pp.19-19
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• 2001

• 한국식물병리학회:학술대회논문집
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• 한국식물병리학회 2002년도 총회 및 추계학술발표회
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• pp.49.1-49
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• 2002

• 한국식물병리학회:학술대회논문집
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• 한국식물병리학회 2002년도 총회 및 추계학술발표회
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• pp.48-49
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• 2002

• 한국식물생명공학회:학술대회논문집
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• 한국식물생명공학회 2002년도 춘계학술대회
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• pp.168-168
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• 2002

• 한국식품조리과학회지
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• 제22권2호
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• pp.140-146
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• 2006

The sensory characteristics of bread prepared with the addition of Angelica plant(Bakluncho) and Jujube(Daechu) powders were investigated The moisture, crude protein, as reducing sugar and vitamin C content of Angelica plant(Bakluncho) powders were 7.78%, 6.07%, 7.37%, 6.13% and 50.10 mg% respectively, and those of Jujube(Daechu) powders were 11.19%, 4.43%, 2.36%, 14.23% and 49.20 mg% respectively. Lightness value decreased but redness and yellowness values increased with increasing natural pigment powders content. The mechanical hardness of the bread decreased with the addition of 3% Angelica plant(Bakluncho) powders, but increased with the addition of 1% and 5% Angelica plant(Bakluncho) powders. The mechanical hardness of bread decreased with the addition of 1% and 3% Jujube(Daechu) powders, but increased with the addition of 5% Jujube(Daechu) powders. In sensory characteristics, the crust color, mb color, moistness and springiness decreased, but aroma and hardness increased with the increasing natural pigment powders content. The savory taste and overall quality of breads with 1% Angelica plant(Bakluncho) powders and 3% Jujube(Daechu) powders were higher than those of the control without my addition. A negative correlation was observed between Hunter's color value and overall quality of the bread prepared with addition of Angelica plant(Bakluncho) and Jujube(Daechu) powders.

• The Plant Pathology Journal
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• 제30권2호
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• pp.151-158
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• 2014

Three double-stranded RNAs (dsRNAs), approximately 1.85, 1.65 and 1.27 kb in size, were detected in an isolate of Cytospora sacchari from Iran. Partial nucleotide sequence revealed a 1,284 bp segment containing one ORF that potentially encodes a 405 aa protein. This protein contains conserved motifs related to RNA dependent RNA polymerases (RdRp) that showed similarity to RdRps of partitiviruses. The results indicate that these dsRNAs represent a novel Partitivirus that we tentatively designate Cytospora sacchari partitivirus (CsPV). Treatment of the fungal strain by cyclohexamide and also hyphal tip culture had no effect on removing the putative virus. Phylogenetic analysis of putative RdRp of CsPV and other partitiviruses places CsPV as a member of the genus Partitivirus in the family Partitiviridae, and clustering with Aspergillus ochraceous virus 1.

• Food Science and Biotechnology
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• 제18권3호
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• pp.661-666
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• 2009

The heat tolerance and the inactivation kinetics of peroxidase (POD) and polyphenol oxidase (PPO) in pineapples (Ananas comosus) were studied in the temperature range $45-95^{\circ}C$. The kinetic parameters, such as deactivation rate constant (k), activation energy ($E_a$), and decimal reduction rate (D) of the thermal inactivation process, were determined. POD in pineapples showed biphasic inactivation behavior at temperatures range $45-75^{\circ}C$ but was monophasic at $85-95^{\circ}C$. This indicate that POD has 2 isozymes, namely heat labile and heat resistant, with $E_a$ of 68.79 and 93.23 kJ/mol, respectively. On the other hand, the heat denaturation of pineapple PPO could be described as simple monophasic first-order behavior with $E_a$ of 80.15 kJ/mol. Thus, the results of this study is useful in blanching technology where it shows a shortened time with higher temperature can be applied. The determination of the heat tolerance and inactivation POD and PPO, at different temperature range as done in the present work, was very important to improve the blanching process. This also will help to optimize the pineapple canning process which is one of the most important food industries in many tropical regions.

• Journal of Plant Biotechnology
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• 제37권3호
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• pp.262-268
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• 2010

Antibodies are powerful and versatile tools to play a critical role in the diagnosis and treatment of many diseases. Their application has been enhanced significantly with the advanced recombinant DNA and heterologonous expression technologies, allowing to produce immunotherapeutic proteins with improved biofunctional properties. However, with currently available technologies, mammalian cell-based therapeutic antibody production, as an alternative for production in humans and animals, is often not plentiful for passive immunotherapeutics in treatment of many diseases. Recently, plant expression systems for therapeutic antibodies have become well-established. Thus, plants have been considered to provide an attractive alternative production system for therapeutic antibodies, as plants have several advantages such as the lack of human pathogens, and low cost of upstream production and flexible scale-up of highly valuable recombinant glycoproteins. Recent advances in modification of posttranslational processing for human-like glycosylation in transgenic plants will make it possible that plant can become a suitable protein expression system over the animal cellbased current production system. This review will discuss recent advances in plant expression technology and issues for their application to therapeutic antibody production.

• 한국환경농학회지
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• 제30권4호
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• pp.390-394
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• 2011

BACKGROUND: Plant expression system for mass production of recombinant proteins has several advantages over other existing expression systems with economical and safety issues. Breast cancer is a cancer originating from breast tissue and comprises almost 25% of all cancers in women world widely. Lewis-Y antigen is difucosylated oligosaccharide and is carried by glycoconjugates at cancer cell surface. In this study, the anti-breast cancer mAb BR55, which recognizes the epitope Lewis-Y, was expressed in the plant expression system. METHODS AND RESULTS: We have developed plant system for production of mAb BR55 with or without KDEL (the ER retention signal). This ER retention signal was attached to C-terminus of protein to help retain the recombinant glycoprotein carrying oligomannose glycans and enhance glycoprotein accumulation. PCR analysis was performed and confirmed the presence of recombinant genes. Western blot validated that the recombinant proteins mAb BR55 with or without KDEL were expressed in transgenic plants, moreover, the expression level of the mAb BR55 with KDEL was higher compared to the mAb BR55 without KDEL. CONCLUSION: These results indicate that KDEL fusion is a good way to produce proteins and plant can be an ideal expression system to obtain proteins and enhance accumulation of proteins.